Text Search >
Deuterium+oxide
Print…
You Searched For:
8,743 results were found
Deuterium+oxide
Catalog Number:
(AA11655-30)
Supplier:
Thermo Scientific Chemicals
Description:
Reagent Grade,UN1455,Crystalline,DANGER: OXIDIZER, causes GI injury, skin and eye irritation,1kg,250g,OXIDIZER,
Supplier:
BeanTown Chemical
Description:
CAS: 1303-86-2; EC No: 215-125-8; MDL No: MFCD00011315; RTECS: ED7900000
-60 Mesh Powder; Molecular Formula: B2O3; MW: 69.62
Melting Point: 45°
Density (g/mL): 2.46
Hygroscopic
Catalog Number:
(77512-442)
Supplier:
AFG BIOSCIENCE LLC
Description:
Human NOS3 (Nitric Oxide Synthase 3, Endothelial) ELISA Kit
Catalog Number:
(10481-416)
Supplier:
Bioss
Description:
Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidized to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidized to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidized Prx can be reduced back to the active form during recovery after oxidative stress.
Catalog Number:
(80600-348)
Supplier:
MilliporeSigma
Description:
A cell-permeable, photo-stable nitric oxide (NO) fluorescent indicator with a detection limit of ~3 nM.
Catalog Number:
(10481-410)
Supplier:
Bioss
Description:
Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidized to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidized to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidized Prx can be reduced back to the active form during recovery after oxidative stress.
Supplier:
Sartorius
Description:
Minisart NML standard syringe filter for clarification and sterilization of liquids and gases.
Supplier:
G-Biosciences
Description:
Many commercial grade detergents contain elevated levels of sulfhydryl oxidizing agents, peroxides, salts and carbonyl compounds
Catalog Number:
(10102-546)
Supplier:
Prosci
Description:
RDH16 is an oxidoreductase with a preference for NAD. It oxidizes all-trans-retinol and 13-cis-retinol to the corresponding aldehydes. RDH16 has higher activity towards CRBP-bound retinol than with free retinol. It also oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. RDH16 can also catalyze the reverse reaction.
Catalog Number:
(77440-644)
Supplier:
Bioss
Description:
This gene encodes an enzyme that belongs to the family of dihydrodiol dehydrogenases, which exist in multiple forms in mammalian tissues and are involved in the metabolism of xenobiotics and sugars. These enzymes catalyze the NADP1-linked oxidation of transdihydrodiols of aromatic hydrocarbons to corresponding catechols. This enzyme is a dimeric dihydrodiol dehydrogenase, and it differs from monomeric dihydrodiol dehydrogenases in its high substrate specificity for trans-dihydrodiols of aromatic hydrocarbons in the oxidative direction. [provided by RefSeq, Jul 2008]
Catalog Number:
(10360-618)
Supplier:
Bioss
Description:
Plays an essential role in the mitochondrial beta-oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA.
Supplier:
HiMedia
Description:
TMAO (Trimethylamine-N-Oxide Medium) medium is used for the cultivation and differentiation of Campylobacter species from foods, except <i>C. jejuni </i>and <i>C. coli</i> in accordance with APHA.
Catalog Number:
(10103-964)
Supplier:
Prosci
Description:
ADHFE1 is hydroxyacid-oxoacid transhydrogenase, which is responsible for the oxidation of 4-hydroxybutyrate in mammalian tissues.The ADHFE1 gene encodes hydroxyacid-oxoacid transhydrogenase (EC 1.1.99.24), which is responsible for the oxidation of 4-hydroxybutyrate in mammalian tissues (Kardon et al., 2006 [PubMed 16616524]).
Supplier:
Thermo Scientific Chemicals
Description:
Cytotoxic compound that causes oxidative base damage to nuclear DNA
Catalog Number:
(10435-136)
Supplier:
Bioss
Description:
Aldehydic products of lipid peroxidation, such as 4 hydroxynonenal (4 HNE), have been implicated in the etiology of pathological changes under oxidative stress as a key mediator of oxidative stress induced cell death. It is a stable product of lipid peroxidation, is proarrhythmic and may contribute to the cytotoxic effects of oxidative stress
4-HNE has been hypothesized to play a key role in cell signal transduction, in a variety of pathways from cell cycle events to cellular adhesion.
Supplier:
Teknova
Description:
DNase, RNase and Protease tested Teknova Cell Culture Grade Water.
Inquire for Price
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
 is still displayed and you need assistance, please call us at 1-800-932-5000.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
is still displayed and you need assistance, please call us at 1-800-932-5000.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
This product has been blocked by your organization. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
This product is no longer available. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service at 1-800-932-5000.
|
|||||||||
List View
